Y. C. Gladish

Bio: Y. C. Gladish is an academic researcher. The author has contributed to research in topics: Monoamine oxidase & Pargyline. The author has an hindex of 2, co-authored 2 publications receiving 124 citations.

New inhibitor of monoamine oxidase.

Abstract: THE following is the initial report of a structurally unique monoamine oxidase inhibitor, N-benzyl-N-methyl-2-propynylamine hydrochloride (A19120). This work includes in vitro action of this inhibitor on rat liver mitochondria as well as in vivo inhibition of monoamine oxidase of mouse brain and the liver.

Structure-activity relations in the pargyline series.

Abstract: Benzaldehyde is condensed with methylamine to give a Schiff base, which, in turn, is hydrogenated with palladium on charcoal to give benzylmethylamine. This is alkylated with propargyl bromide to yield pargyline. We were quite fortunate that soon after we inaugurated our search for a nonhydrazine M A 0 inhibitor, Taylor and Wykes devised a rapid in uitro screening method. This method was reported at the Federation Proceedings in March, 1959.' It is based upon the production of a dark brown pigment through the action of the M A 0 enzyme on the substrate serotonin. Graded levels of inhibitors roduced corresponding graded responses in

Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase.

Abstract: A novel enzyme responsible for the oxidation of spermidine and spermine has been found in rat liver. Spermidine is shown to be degraded to putrescine and 3-aminopropionaldehyde, and spermine to be cleaved to spermidine and 3-aminopropionaldehyde. A single enzyme catalyzing both reactions and designated as polyamine oxidase has been purified 4000-fold to electrophoretic homogeneity. Polyamine oxidase appears to be a flavoprotein, containing flavin adenine dinucleotide (FAD) as a prosthetic group. Hydrogen peroxide is evolved in the reaction and no other electron acceptors except molecular oxygen have been found. The molecular weight of the enzyme was approximately 60 000 and the sedimentation coefficient 4.5 S. The enzyme appears to be a single polypeptide chain since no evidence for structural subunits was obtained. Polyamine oxidase was sensitive to sulfhydryl and carbonyl group reagents. The optimum pH value for the oxidation of polyamines was close to 10. The reaction velocities were enhanced by various aldehydes, especially certain aromatic aldehydes. Polyamine oxidase appears to be localized in peroxisomes of liver cells, although the existence of an isoenzyme in the cytosolic fraction was not definitively ruled out. No marked changes were observed in the activity of polyamine oxidase in rat liver after partial hepatectomy, carbon tetrachloride poisoning, and after treatment with growth hormone or thioacetamide, conditions which are known to alter profoundly the metabolism and accumulation of polyamines.

Multiple Forms of Human Brain Mitochondrial Monoamine Oxidase

Abstract: Monoamine oxidase exists in at least four molecular forms in different areas of the human brain. Variations in their enzymatic properties may have important clinical implications, perhaps reflecting their relative ability to degrade different monoamine substrates in vivo.

Multiple Forms of Rat Brain Monoamine Oxidase

Abstract: THE enzyme monoamine oxidase (monoamine : O2 oxido-reductase (deaminating), EC 1.4.3.4) (MAO) is likely to be concerned in the metabolism of known or suspected central nervous system transmitters such as nor adrenaline, dopamine and 5-hydroxytryptamine. In the therapy of depressive disease, drugs are used which are able to inhibit MAO and it is thought that they owe their beneficial effect to this ability and to the resulting accumulation of amines. It is found, however, that some compounds belonging to this group are considerably more effective therapeutically than others1,2 and no fully satisfactory explanation has been offered. We now offer an approach which we think in better accord with the characteristics of MAO.